The objective of this project is to elucidate the processes whereby proteins form unique native conformations and function selectively in solution. The method of choice is nuclear magnetic resonance (NMR) applied to directly observe resonances of individual atoms within the protein molecule. Most work to date has concentrated on the histidine C2 proton resonances as the only singly resolved proton resonances of a series of small stable proteins, e.g. ribonuclease, cytochrome c, myoglobin, using proton NMR. Recently we have been able to resolve for the first time the individual carboxyl carbon atoms of hen egg white lysozyme using carbon-13 NMR at natural abundance of C13 (1.1%). Current and projected work includes the extension of these approaches to larger proteins, hemoglobin and protein hormones.